Solid state NMR spectroscopy will be used to study polycrystalline and amorphous peptides. The conformation and dynamics of peptides specifically synthesized to have well defined structural features in the solid state will be described. This new research on peptides in the solid state will be complementary to on going research on these same peptides in solution and allow important questions about the differences in conformation in solutions and in crystals to be answered. Several of the NMR experiments give unique information; in particular the details of bond geometries from 13C-14N dipolar couplings and 13C isotropic chemical shifts, the existence of asymmetric or multiple conformations from 13C chemical shifts and the dynamics of aromatic rings from the averaging of 2H quadrupole and 13C chemical shift powder patterns. The use of these peptides as model compounds for biological solid state NMR will lead to further development of the techniques and instrumentation.